Evidence map›Paper›PMID 15928345›Full record

ArticleRNA (New York, N.Y.)2005

RNA chaperone activity of protein components of human Ro RNPs.

Aurélia Belisova, Katharina Semrad, Oliver Mayer, Grazia Kocian, Elisabeth Waigmann, Renée Schroeder, Günter Steiner

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.1field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

35 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. Structure ofRNA biology · 2021
    Article
  3. Review
  4. Review
  5. Review
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Functional roles of non-coding Y RNAs.The international journal of biochemistry & cell biology · 2015
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Clinical and pathological roles of Ro/SSA autoantibody system.Clinical & developmental immunology · 2012
    Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 2 institutions in 1 country.

Aurélia BelisovaDepartment of Medical Biochemistry, Medical University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, A-1030 Vienna, Austria.
Katharina Semrad
Oliver Mayer
Grazia Kocian
Elisabeth Waigmann
Renée Schroeder
Günter Steiner
Max Perutz Labs · ATVienna Biocenter · AT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ro ribonucleoprotein (RNP) complexes are composed of one molecule of a small noncoding cytoplasmic RNA, termed Y RNA, and the two proteins Ro60 and La. Additional proteins such as hnRNP I, hnRNP K, or nucleolin have recently been shown to be associated with subpopulations of Y RNAs. Ro RNPs appear to be localized in the cytoplasm of all higher eukaryotic cells but their functions have remained elusive. To shed light on possible functions of Ro RNPs, we tested protein components of these complexes for RNA chaperone properties employing two in vitro chaperone assays and additionally an in vivo chaperone assay. In these assays the splicing activity of a group I intron is measured. La showed pronounced RNA chaperone activity in the cis-splicing assay in vitro and also in vivo, whereas no activity was seen in the trans-splicing assay in vitro. Both hnRNP I and hnRNP K exhibited strong chaperone activity in the two in vitro assays, however, proved to be cytotoxic in the in vivo assay. No chaperone activity was observed for Ro60 in vitro and a moderate activity was detected in vivo. In vitro chaperone activities of La and hnRNP I were completely inhibited upon binding of Y RNA. Taken together, these data suggest that the Ro RNP components La, hnRNP K, and hnRNP I possess RNA chaperone activity, while Ro60-Y RNA complexes might function as transporters, bringing other Y RNA binding proteins to their specific targets.

Indexed as

AutoantigensCytoplasmHeterogeneous-Nuclear RibonucleoproteinsHumansIntronsIn Vitro TechniquesMolecular ChaperonesMutationProtein BindingRecombinant ProteinsRibonucleoproteinsRNARNA, Small CytoplasmicSS-A AntigenSS-B AntigenSulfur RadioisotopesAutoantigensHeterogeneous-Nuclear RibonucleoproteinsMolecular ChaperonesRecombinant ProteinsRibonucleoproteinsRNARNA, Small CytoplasmicRO60 protein, humanSS-A AntigenSS-B AntigenSulfur Radioisotopes

Identifiers

PMID15928345
PMCPMC1370793
OpenAlexW2119312493

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.